ID   D3VDJ3_XENNA            Unreviewed;       410 AA.
AC   D3VDJ3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Broad specificity amino-acid racemase {ECO:0000256|HAMAP-Rule:MF_02212};
DE            EC=5.1.1.10 {ECO:0000256|HAMAP-Rule:MF_02212};
DE   Flags: Precursor;
GN   OrderedLocusNames=XNC1_4208 {ECO:0000313|EMBL:CBJ92233.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS   1036 / NCIMB 9965 / AN6).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ92233.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|EMBL:CBJ92233.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 /
RC   AN6 {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA   Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA   Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA   Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA   Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA   Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA   Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA   van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA   Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA   Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT   convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:E27909-E27909(2011).
CC   -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC       substrates. {ECO:0000256|HAMAP-Rule:MF_02212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:32557; Evidence={ECO:0000256|HAMAP-Rule:MF_02212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC         Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC         EC=5.1.1.10; Evidence={ECO:0000256|HAMAP-Rule:MF_02212};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_02212, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|HAMAP-Rule:MF_02212}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC       {ECO:0000256|ARBA:ARBA00023456, ECO:0000256|HAMAP-Rule:MF_02212}.
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DR   EMBL; FN667742; CBJ92233.1; -; Genomic_DNA.
DR   RefSeq; WP_013185532.1; NC_014228.1.
DR   AlphaFoldDB; D3VDJ3; -.
DR   STRING; 406817.XNC1_4208; -.
DR   KEGG; xne:XNC1_4208; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_6; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR   GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR   GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_02212; Bsr_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR043698; Racemase_Bsr/Lyr.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_02212};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02212};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_02212};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_02212}; Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02212}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
FT   CHAIN           24..410
FT                   /note="Broad specificity amino-acid racemase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
FT                   /id="PRO_5026402156"
FT   DOMAIN          279..407
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         74
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
FT   DISULFID        70..96
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
SQ   SEQUENCE   410 AA;  44703 MW;  B414A1BAB5AA2BD3 CRC64;
     MRLNKTTLAI LLGLSLYQGA AQAAPVLSSD NTQAKRVAAH NNAWVEINTT TFENNIHILQ
     QKLNRNTKMC AVLKGDAYGH GIGLLMPSVI KTGVLCVGIT SNEEARIVRE SGFKGQLIRI
     RTADVSEIES TLGYDMEEII GDLAHAKTVA DLAKKHGKEI RVHLALNTGL MSRNGLEMKT
     EQGKQEALKM TQLPNLKLVG IMSHHALTDL DAIRDSIKNF NEQTAWLIKA ANLKRDEITL
     HASSSFASVS IPEAQFDMVR VGSALYGILT NTHPEFKPLI QVKTHVASVK SYPKGNGVSY
     NNTYILKRDS KLANLPVGFS DGFSSSLSNK AYVLINGHRA PVVGSVSMNT VMADVTDLPE
     VKSGDEVVIF GKQGNEEITQ SDIQKWGGMH VVEFSSIWGE TNPRIVTTDA
//